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Q8WWW0 (RASF5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras association domain-containing protein 5
Alternative name(s):
New ras effector 1
Regulator for cell adhesion and polarization enriched in lymphoid tissues
Short name=RAPL
Gene names
Name:RASSF5
Synonyms:NORE1, RAPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis. Ref.2 Ref.9 Ref.11

Subunit structure

Interacts directly with activated HRAS; a RASSF5-STK4/MST1 complex probably associates with activated HRAS. Interacts with KRAS. Probably interacts with Ras-like GTPases RRAS, RRAS2, MRAS, RAP1B, RAP2A and RALA. Can self-associate. Interacts with RSSF1 isoform A The RSSF1 isoform A-RSSF5heterodimer probably mediates the association of RSSF1 with HRAS By similarity. Isoform 2 interacts with activated RAP1A and ITGAL/LFA-1. Binds STK4/MST1, inhibiting STK4/MST1 autoactivation. Ref.2 Ref.10 Ref.11

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Note: Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells. Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological synapse. Isoform 2 is localized to growing microtubules in vascular endothelial cells and is dissociated from microtubules by activated RAP1A. Ref.2 Ref.11

Tissue specificity

Widely expressed. Frequently down-regulated in lung tumor cell lines and primary lung tumors. Ref.1 Ref.9

Sequence similarities

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 Ras-associating domain.

Contains 1 SARAH domain.

Caution

Was termed (Ref.3) RASSF3.

Sequence caution

The sequence AAH04270.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH04270.1 differs from that shown. Reason: Aberrant splicing.

The sequence AAH07203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH07203.1 differs from that shown. Reason: Aberrant splicing.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WWW0-1)

Also known as: A; NORE1A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8WWW0-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     154-193: CKFTCHPECR...ESTLTVTFSQ → MTVDSSMSSG...RNAQSKHLSK
Note: Initiator Met-1 is removed. Contains a N-acetylthreonine at position 2.
Isoform 3 (identifier: Q8WWW0-3)

Also known as: C; NORE1B;

The sequence of this isoform differs from the canonical sequence as follows:
     331-336: LFQKLS → GCLLHP
     337-418: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Ras association domain-containing protein 5
PRO_0000240401

Regions

Domain274 – 36491Ras-associating
Domain366 – 41348SARAH
Zinc finger122 – 17049Phorbol-ester/DAG-type

Amino acid modifications

Modified residue3521Phosphothreonine Ref.12 Ref.13

Natural variations

Alternative sequence1 – 153153Missing in isoform 2.
VSP_019363
Alternative sequence154 – 19340CKFTC…VTFSQ → MTVDSSMSSGYCSLDEELED CFFTAKTTFFRNAQSKHLSK in isoform 2.
VSP_019364
Alternative sequence331 – 3366LFQKLS → GCLLHP in isoform 3.
VSP_019365
Alternative sequence337 – 41882Missing in isoform 3.
VSP_019366

Secondary structure

..... 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) (NORE1A) [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 4AFBC69B1325CC9E

FASTA41847,090
        10         20         30         40         50         60 
MAMASPAIGQ RPYPLLLDPE PPRYLQSLSG PELPPPPPDR SSRLCVPAPL STAPGAREGR 

        70         80         90        100        110        120 
SARRAARGNL EPPPRASRPA RPLRPGLQQR LRRRPGAPRP RDVRSIFEQP QDPRVPAERG 

       130        140        150        160        170        180 
EGHCFAELVL PGGPGWCDLC GREVLRQALR CTNCKFTCHP ECRSLIQLDC SQQEGLSRDR 

       190        200        210        220        230        240 
PSPESTLTVT FSQNVCKPVE ETQRPPTLQE IKQKIDSYNT REKNCLGMKL SEDGTYTGFI 

       250        260        270        280        290        300 
KVHLKLRRPV TVPAGIRPQS IYDAIKEVNL AATTDKRTSF YLPLDAIKQL HISSTTTVSE 

       310        320        330        340        350        360 
VIQGLLKKFM VVDNPQKFAL FKRIHKDGQV LFQKLSIADR PLYLRLLAGP DTEVLSFVLK 

       370        380        390        400        410 
ENETGEVEWD AFSIPELQNF LTILEKEEQD KIQQVQKKYD KFRQKLEEAL RESQGKPG 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 66AD5D84EFA6D6CB
Show »

FASTA26530,359
Isoform 3 (C) (NORE1B) [UniParc].

Checksum: 2657B6DAECD8D6A9
Show »

FASTA33637,433

References

« Hide 'large scale' references
[1]"RASSF3 and NORE1: identification and cloning of two human homologues of the putative tumor suppressor gene RASSF1."
Tommasi S., Dammann R., Jin S.-G., Zhang X.-F., Avruch J., Pfeifer G.P.
Oncogene 21:2713-2720(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[2]"RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1."
Katagiri K., Maeda A., Shimonaka M., Kinashi T.
Nat. Immunol. 4:741-748(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INTEGRIN ACTIVATION, INTERACTION WITH RAP1A AND ITGAL, SUBCELLULAR LOCATION.
[3]"RASSF3 is regulated by methylation in lung and breast tumor cell lines."
Burbee D.G., White M.A., Minna J.D.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Lymph node.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Skin.
[9]"The pro-apoptotic Ras effector Nore1 may serve as a Ras-regulated tumor suppressor in the lung."
Vos M.D., Martinez A., Ellis C.A., Vallecorsa T., Clark G.J.
J. Biol. Chem. 278:21938-21943(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TUMOR SUPPRESSOR, TISSUE SPECIFICITY.
[10]"Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras."
Praskova M., Khoklatchev A., Ortiz-Vega S., Avruch J.
Biochem. J. 381:453-462(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STK4/MST1.
[11]"Local activation of Rap1 contributes to directional vascular endothelial cell migration accompanied by extension of microtubules on which RAPL, a Rap1-associating molecule, localizes."
Fujita H., Fukuhara S., Sakurai A., Yamagishi A., Kamioka Y., Nakaoka Y., Masuda M., Mochizuki N.
J. Biol. Chem. 280:5022-5031(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MICROTUBULE GROWTH REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH RAP1A.
[12]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF445801 mRNA. Translation: AAL38592.1.
AY261332 mRNA. Translation: AAP83360.1.
AY062002 mRNA. Translation: AAL40388.1.
AY062003 mRNA. Translation: AAL40389.1.
AY216268 mRNA. Translation: AAO61668.1.
AK289861 mRNA. Translation: BAF82550.1.
AL832784 mRNA. Translation: CAI46164.1.
AL591846, AL354681 Genomic DNA. Translation: CAI13536.1.
AL591846, AL354681 Genomic DNA. Translation: CAI13538.1.
AL354681, AL591846 Genomic DNA. Translation: CAI15252.1.
AL591846, AL354681 Genomic DNA. Translation: CAI13537.1.
AL591846, AL354681 Genomic DNA. Translation: CAI13542.1.
AL354681, AL591846 Genomic DNA. Translation: CAI15253.1.
AL354681, AL591846 Genomic DNA. Translation: CAI15254.1.
AL354681, AL591846 Genomic DNA. Translation: CAI15256.1.
CH471100 Genomic DNA. Translation: EAW93544.1.
BC004270 mRNA. Translation: AAH04270.1. Sequence problems.
BC007203 mRNA. Translation: AAH07203.1. Sequence problems.
BC042651 mRNA. Translation: AAH42651.1.
CCDSCCDS1463.1. [Q8WWW0-3]
CCDS1464.1. [Q8WWW0-2]
CCDS30998.1. [Q8WWW0-1]
RefSeqNP_872604.1. NM_182663.3. [Q8WWW0-1]
NP_872605.1. NM_182664.3. [Q8WWW0-3]
NP_872606.1. NM_182665.3. [Q8WWW0-2]
UniGeneHs.497579.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LGDX-ray3.05E/F/G/H365-413[»]
ProteinModelPortalQ8WWW0.
SMRQ8WWW0. Positions 113-170, 205-362, 366-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123689. 29 interactions.
DIPDIP-32490N.
IntActQ8WWW0. 30 interactions.
STRING9606.ENSP00000347443.

PTM databases

PhosphoSiteQ8WWW0.

Polymorphism databases

DMDM74751587.

Proteomic databases

MaxQBQ8WWW0.
PaxDbQ8WWW0.
PRIDEQ8WWW0.

Protocols and materials databases

DNASU83593.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000304534; ENSP00000306091; ENSG00000136653. [Q8WWW0-2]
ENST00000355294; ENSP00000347443; ENSG00000136653. [Q8WWW0-1]
ENST00000367117; ENSP00000356084; ENSG00000136653. [Q8WWW0-3]
ENST00000577571; ENSP00000462576; ENSG00000266094. [Q8WWW0-2]
ENST00000579436; ENSP00000462099; ENSG00000266094. [Q8WWW0-1]
ENST00000580449; ENSP00000462544; ENSG00000266094. [Q8WWW0-3]
GeneID83593.
KEGGhsa:83593.
UCSCuc001hed.3. human. [Q8WWW0-1]
uc001hee.3. human. [Q8WWW0-3]
uc001hef.3. human. [Q8WWW0-2]

Organism-specific databases

CTD83593.
GeneCardsGC01P206680.
HGNCHGNC:17609. RASSF5.
HPACAB022664.
MIM607020. gene.
neXtProtNX_Q8WWW0.
PharmGKBPA134958571.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308852.
HOGENOMHOG000013025.
HOVERGENHBG054362.
InParanoidQ8WWW0.
KOK08015.
OMANCLLMKL.
OrthoDBEOG7TF796.
PhylomeDBQ8WWW0.
TreeFamTF319243.

Enzyme and pathway databases

SignaLinkQ8WWW0.

Gene expression databases

ArrayExpressQ8WWW0.
BgeeQ8WWW0.
CleanExHS_RASSF5.
GenevestigatorQ8WWW0.

Family and domain databases

InterProIPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000159. Ras-assoc.
IPR011524. SARAH_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamPF00130. C1_1. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]
SMARTSM00109. C1. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS50200. RA. 1 hit.
PS50951. SARAH. 1 hit.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRASSF5.
GenomeRNAi83593.
NextBio72517.
PROQ8WWW0.
SOURCESearch...

Entry information

Entry nameRASF5_HUMAN
AccessionPrimary (citable) accession number: Q8WWW0
Secondary accession number(s): A8K1E6 expand/collapse secondary AC list , Q5SY32, Q8WWV9, Q8WXF4, Q9BT99
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM